› 5yk2

X-ray diffraction
2.81Å resolution

The complex structure of Rv3197-erythromycin from Mycobacterium tuberculosis

Released:
DOI: 10.2210/pdb5yk2/pdb
PDB entry 5yk2 coloured by chain, front view.
PDB entry 5yk2 coloured by chain, side view.
PDB entry 5yk2 coloured by chain, top view.
Source organism: Mycobacterium tuberculosis H37Rv
Primary publication:
Discovery of the first macrolide antibiotic binding protein in Mycobacterium tuberculosis: a new antibiotic resistance drug target.
Zhang Q, Liu H, Liu X, Jiang D, Zhang B, Tian H, Yang C, Guddat LW, Yang H, Mi K, Rao Z
Protein Cell 9 971-975 (2018)
PMID: 29350349

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129433 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ABC1 atypical kinase-like domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 452 amino acids
Theoretical weight: 49.6 KDa
Source organism: Mycobacterium tuberculosis H37Rv
Expression system: Escherichia coli
UniProt:
  • Canonical: O53343 (Residues: 1-447; Coverage: 100%)
Gene name: Rv3197
Sequence domains: ABC1 atypical kinase-like domain

Ligands and Environments

1 bound ligand:
Ligand ERY 1 x ERY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL19U1
Spacegroup: P6322
Unit cell:
a: 187.238Å b: 187.238Å c: 67.205Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.232 0.229 0.274
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Emerging roles of the αC-β4 loop in protein kinase structure, function, evolution, and disease.
Yeung et al. (2020)
1 more